Acyl-CoA-dependent O-acyltransferases catalyze reactions in which fatty acyl-CoAs are joined to acyl acceptors containing free hydroxyl groups to produce neutral lipids. In this report, we characterize a human multifunctional O-acyltransferase (designated MEAT) that belongs to the acyl-CoA:diacylglycerol acyltransferase 2/acyl-CoA:monoacylglycerol acyltransferase (MGAT) gene family and is highly expressed in the skin. Membranes of insect cells and homogenates of mammalian cells overexpressing MEAT exhibited significantly increased MGAT, acyl-CoA:fatty acyl alcohol acyltransferase (wax synthase), and acyl-CoA:retinol acyltransferase (ARAT) activities, which catalyze the synthesis of diacylglycerols, wax monoesters, and retinyl esters, respectively. Furthermore, when provided with the appropriate substrates, intact mammalian cells overexpressing MEAT accumulated more waxes and retinyl esters than control cells. We conclude that MEAT is a multifunctional acyltransferase that likely plays an important role in lipid metabolism in human skin. Copyright © 2005 by the American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Yen, C. L. E., Brown IV, C. H., Monetti, M., & Farese, R. V. (2005). A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. Journal of Lipid Research, 46(11), 2388–2397. https://doi.org/10.1194/jlr.M500168-JLR200
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